規格:100ul
研究領域:細胞生(shēng)物 神經生(shēng)物學 信号轉導 細胞凋亡 Alzheimer's
抗體(tǐ)來(lái)源:Mouse
克隆類型:Polyclonal
交叉反應:Rat,
(predicted: Human, Mouse, Chicken, Dog, Pig, Cow, Rabbit, )
産品應用:ICC=1:50-200 IF=1:50-200
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量:4.4kDa
性 狀:Lyophilized or Liquid
濃 度:1mg/ml
免 疫 原:KLH conjugated synthetic peptide derived from human beta-Amyloid
亞 型:IgG
純化方法:affinity purified by Protein A
儲 存 液:0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
保存條件:Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
産品介紹:background:The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid antibodies and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
Function:Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons.
Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity.
Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brai.
The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.
N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).
Subunit:Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and, NUMB and DAB. Binding to DAB1 inhibits its serine phosphorylation (By similarity). Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Interacts with CPEB1 and AGER. Interacts with ANKS1B and TNFRSF21. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; this is promoted by heparin binding.
Subcellular Location:Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment.
Tissue Specificity:Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra-striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes.
Post-translational modifications:Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59).
Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides.
N- and O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region.
Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin.
Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu(+) complex in the presence of hydrogen peroxide results in an increased production of beta-amyloid-containing peptides.
Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP).
Beta-amyloid peptides are degraded by IDE.
DISEASE:Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:104300]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.
Defects in APP are the cause of amyloidosis cerebroarterial Dutch type (AMYLCAD) [MIM:605714]; also known as hereditary cerebral hemorrhage with amyloidosis Dutch type (HCHWAD). AMYLCAD is a hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. Beta-APP40 is the predominant form of cerebrovascular amyloid. Amyloid is not found outside the nervous system. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Onset of the disease is in middle age (44 to 60 years). Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease.
Defects in APP are the cause of amyloidosis cerebroarterial Italian type (AMYLCAIT) [MIM:605714]. AMYLCAIT is a hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels, resulting in cerebral amyloid angiopathy. Amyloid is not found outside the nervous system. It is a condition very similar to AMYLCAD, but the clinical course is less severe. Patients manifest mild cognitive decline, recurrent strokes, and epilepsy in some cases. There are extensive amyloid deposits in leptomeningeal and cortical vessels and, to a lesser extent, in the neuropil of the cerebral cortex, in the absence of neurofibrillary tangles.
Defects in APP are the cause of amyloidosis cerebroarterial Iowa type (AMYLCAIW) [MIM:605714]. AMYLCAIW is a hereditary amyloidosis due to amyloid-beta A4 peptide(s) deposition. Patients have progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.
Similarity:Belongs to the APP family. Contains 1 BPTI/Kunitz inhibitor domain.
Database links:
Entrez Gene: 351 Human
Entrez Gene: 11820 Mouse
Entrez Gene: 54226 Rat
Omim: 104760 Human
SwissProt: P05067 Human
SwissProt: P12023 Mouse
SwissProt: P08592 Rat
Unigene: 434980 Human
Unigene: 277585 Mouse
Unigene: 2104 Rat
Important Note:This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
111β-Amyloid 也稱β-A4 蛋白、Aβ1-42,是β-澱粉樣蛋白前體(tǐ)(APP)經β和(hé)γ分泌酶分解後的産物,有(yǒu)39-43個(gè)氨基酸殘基組成。是澱粉樣蛋白的主要成分。此蛋白在大(dà)腦(nǎo)中形成不容性的沉積物(老年斑),從而具有(yǒu)特殊的AD,Down's綜合症和(hé)老年癡呆症的形态學特征。β-澱粉樣蛋白來(lái)自β-澱粉樣蛋白原,在腦(nǎo)組織的細胞外呈絲狀蛋白樣沉積,是澱粉樣結節性神經炎病變的主要蛋白成分,在神經纖維中也有(yǒu)沉積。
在老年性癡呆Alzheimer病中,大(dà)腦(nǎo)皮質中特征性地出現β-澱粉樣蛋白沉積形成的老年斑。主要用于老年性癡呆症病人(rén)大(dà)腦(nǎo)組織噬斑中澱粉樣物質的檢測。必要時(shí)石蠟組織切片用98-100%甲酸處理(lǐ)2-3分鍾。
222
研究領域:細胞生(shēng)物 神經生(shēng)物學 信号轉導 細胞凋亡 Alzheimer's
抗體(tǐ)來(lái)源:Mouse
克隆類型:Polyclonal
交叉反應:Rat,
(predicted: Human, Mouse, Chicken, Dog, Pig, Cow, Rabbit, )
産品應用:ICC=1:50-200 IF=1:50-200
not yet tested in other applications.
optimal dilutions/concentrations should be determined by the end user.
分 子 量:4.4kDa
性 狀:Lyophilized or Liquid
濃 度:1mg/ml
免 疫 原:KLH conjugated synthetic peptide derived from human beta-Amyloid
亞 型:IgG
純化方法:affinity purified by Protein A
儲 存 液:0.01M TBS(pH7.4) with 1% BSA, 0.03% Proclin300 and 50% Glycerol.
保存條件:Store at -20 °C for one year. Avoid repeated freeze/thaw cycles. The lyophilized antibody is stable at room temperature for at least one month and for greater than a year when kept at -20°C. When reconstituted in sterile pH 7.4 0.01M PBS or diluent of antibody the antibody is stable for at least two weeks at 2-4 °C.
産品介紹:background:The cerebral and vascular plaques associated with Alzheimer's disease are mainly composed of Amyloid beta peptides. beta Amyloid is derived from cleavage of the Amyloid precursor protein and varies in length from 39 to 43 amino acids. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides result from cleavage of Amyloid precursor protein after residues 40, 42, and 43, respectively. The cleavage takes place by gamma-secretase during the last Amyloid precursor protein processing step. beta Amyloid [1-40], beta Amyloid [1-42], and beta Amyloid [1-43] peptides are major constituents of the plaques and tangles that occur in Alzheimer's disease. beta Amyloid antibodies and peptides have been developed as tools for elucidating the biology of Alzheimer's disease.
Function:Functions as a cell surface receptor and performs physiological functions on the surface of neurons relevant to neurite growth, neuronal adhesion and axonogenesis. Involved in cell mobility and transcription regulation through protein-protein interactions. Can promote transcription activation through binding to APBB1-KAT5 and inhibits Notch signaling through interaction with Numb. Couples to apoptosis-inducing pathways such as those mediated by G(O) and JIP. Inhibits G(o) alpha ATPase activity. Acts as a kinesin I membrane receptor, mediating the axonal transport of beta-secretase and presenilin 1. Involved in copper homeostasis/oxidative stress through copper ion reduction. In vitro, copper-metallated APP induces neuronal death directly or is potentiated through Cu(2+)-mediated low-density lipoprotein oxidation. Can regulate neurite outgrowth through binding to components of the extracellular matrix such as heparin and collagen I and IV. The splice isoforms that contain the BPTI domain possess protease inhibitor activity. Induces a AGER-dependent pathway that involves activation of p38 MAPK, resulting in internalization of amyloid-beta peptide and leading to mitochondrial dysfunction in cultured cortical neurons.
Beta-amyloid peptides are lipophilic metal chelators with metal-reducing activity. Bind transient metals such as copper, zinc and iron. In vitro, can reduce Cu(2+) and Fe(3+) to Cu(+) and Fe(2+), respectively. Beta-amyloid 42 is a more effective reductant than beta-amyloid 40. Beta-amyloid peptides bind to lipoproteins and apolipoproteins E and J in the CSF and to HDL particles in plasma, inhibiting metal-catalyzed oxidation of lipoproteins. Beta-APP42 may activate mononuclear phagocytes in the brain and elicit inflammatory responses. Promotes both tau aggregation and TPK II-mediated phosphorylation. Interaction with overexpressed HADH2 leads to oxidative stress and neurotoxicity.
Appicans elicit adhesion of neural cells to the extracellular matrix and may regulate neurite outgrowth in the brai.
The gamma-CTF peptides as well as the caspase-cleaved peptides, including C31, are potent enhancers of neuronal apoptosis.
N-APP binds TNFRSF21 triggering caspase activation and degeneration of both neuronal cell bodies (via caspase-3) and axons (via caspase-6).
Subunit:Binds, via its C-terminus, to the PID domain of several cytoplasmic proteins, including APBB family members, the APBA family, MAPK8IP1, SHC1 and, NUMB and DAB. Binding to DAB1 inhibits its serine phosphorylation (By similarity). Also interacts with GPCR-like protein BPP, FPRL1, APPBP1, IB1, KNS2 (via its TPR domains), APPBP2 (via BaSS) and DDB1. In vitro, it binds MAPT via the MT-binding domains. Associates with microtubules in the presence of ATP and in a kinesin-dependent manner. Interacts, through a C-terminal domain, with GNAO1. Amyloid beta-42 binds CHRNA7 in hippocampal neurons. Beta-amyloid associates with HADH2. Soluble APP binds, via its N-terminal head, to FBLN1. Interacts with CPEB1 and AGER. Interacts with ANKS1B and TNFRSF21. Interacts with ITM2B. Interacts with ITM2C. Interacts with IDE. Can form homodimers; this is promoted by heparin binding.
Subcellular Location:Membrane; Single-pass type I membrane protein. Membrane, clathrin-coated pit. Note=Cell surface protein that rapidly becomes internalized via clathrin-coated pits. During maturation, the immature APP (N-glycosylated in the endoplasmic reticulum) moves to the Golgi complex where complete maturation occurs (O-glycosylated and sulfated). After alpha-secretase cleavage, soluble APP is released into the extracellular space and the C-terminal is internalized to endosomes and lysosomes. Some APP accumulates in secretory transport vesicles leaving the late Golgi compartment and returns to the cell surface. Gamma-CTF(59) peptide is located to both the cytoplasm and nuclei of neurons. It can be translocated to the nucleus through association with APBB1 (Fe65). Beta-APP42 associates with FRPL1 at the cell surface and the complex is then rapidly internalized. APP sorts to the basolateral surface in epithelial cells. During neuronal differentiation, the Thr-743 phosphorylated form is located mainly in growth cones, moderately in neurites and sparingly in the cell body. Casein kinase phosphorylation can occur either at the cell surface or within a post-Golgi compartment.
Tissue Specificity:Expressed in all fetal tissues examined with highest levels in brain, kidney, heart and spleen. Weak expression in liver. In adult brain, highest expression found in the frontal lobe of the cortex and in the anterior perisylvian cortex-opercular gyri. Moderate expression in the cerebellar cortex, the posterior perisylvian cortex-opercular gyri and the temporal associated cortex. Weak expression found in the striate, extra-striate and motor cortices. Expressed in cerebrospinal fluid, and plasma. Isoform APP695 is the predominant form in neuronal tissue, isoform APP751 and isoform APP770 are widely expressed in non-neuronal cells. Isoform APP751 is the most abundant form in T-lymphocytes. Appican is expressed in astrocytes.
Post-translational modifications:Proteolytically processed under normal cellular conditions. Cleavage either by alpha-secretase, beta-secretase or theta-secretase leads to generation and extracellular release of soluble APP peptides, S-APP-alpha and S-APP-beta, and the retention of corresponding membrane-anchored C-terminal fragments, C80, C83 and C99. Subsequent processing of C80 and C83 by gamma-secretase yields P3 peptides. This is the major secretory pathway and is non-amyloidogenic. Alternatively, presenilin/nicastrin-mediated gamma-secretase processing of C99 releases the amyloid beta proteins, amyloid-beta 40 (Abeta40) and amyloid-beta 42 (Abeta42), major components of amyloid plaques, and the cytotoxic C-terminal fragments, gamma-CTF(50), gamma-CTF(57) and gamma-CTF(59).
Proteolytically cleaved by caspases during neuronal apoptosis. Cleavage at Asp-739 by either caspase-6, -8 or -9 results in the production of the neurotoxic C31 peptide and the increased production of beta-amyloid peptides.
N- and O-glycosylated. O-linkage of chondroitin sulfate to the L-APP isoforms produces the APP proteoglycan core proteins, the appicans. The chondroitin sulfate chain of appicans contains 4-O-sulfated galactose in the linkage region and chondroitin sulfate E in the repeated disaccharide region.
Phosphorylation in the C-terminal on tyrosine, threonine and serine residues is neuron-specific. Phosphorylation can affect APP processing, neuronal differentiation and interaction with other proteins. Phosphorylated on Thr-743 in neuronal cells by Cdc5 kinase and Mapk10, in dividing cells by Cdc2 kinase in a cell-cycle dependent manner with maximal levels at the G2/M phase and, in vitro, by GSK-3-beta. The Thr-743 phosphorylated form causes a conformational change which reduces binding of Fe65 family members. Phosphorylation on Tyr-757 is required for SHC binding. Phosphorylated in the extracellular domain by casein kinases on both soluble and membrane-bound APP. This phosphorylation is inhibited by heparin.
Extracellular binding and reduction of copper, results in a corresponding oxidation of Cys-144 and Cys-158, and the formation of a disulfide bond. In vitro, the APP-Cu(+) complex in the presence of hydrogen peroxide results in an increased production of beta-amyloid-containing peptides.
Trophic-factor deprivation triggers the cleavage of surface APP by beta-secretase to release sAPP-beta which is further cleaved to release an N-terminal fragment of APP (N-APP).
Beta-amyloid peptides are degraded by IDE.
DISEASE:Defects in APP are the cause of Alzheimer disease type 1 (AD1) [MIM:104300]. AD1 is a familial early-onset form of Alzheimer disease. It can be associated with cerebral amyloid angiopathy. Alzheimer disease is a neurodegenerative disorder characterized by progressive dementia, loss of cognitive abilities, and deposition of fibrillar amyloid proteins as intraneuronal neurofibrillary tangles, extracellular amyloid plaques and vascular amyloid deposits. The major constituent of these plaques is the neurotoxic amyloid-beta-APP 40-42 peptide (s), derived proteolytically from the transmembrane precursor protein APP by sequential secretase processing. The cytotoxic C-terminal fragments (CTFs) and the caspase-cleaved products such as C31 derived from APP, are also implicated in neuronal death.
Defects in APP are the cause of amyloidosis cerebroarterial Dutch type (AMYLCAD) [MIM:605714]; also known as hereditary cerebral hemorrhage with amyloidosis Dutch type (HCHWAD). AMYLCAD is a hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels. Beta-APP40 is the predominant form of cerebrovascular amyloid. Amyloid is not found outside the nervous system. The principal clinical characteristics are recurrent cerebral and cerebellar hemorrhages, recurrent strokes, cerebral ischemia, cerebral infarction, and progressive mental deterioration. Onset of the disease is in middle age (44 to 60 years). Patients develop cerebral hemorrhage because of the severe cerebral amyloid angiopathy. Parenchymal amyloid deposits are rare and largely in the form of pre-amyloid lesions or diffuse plaque-like structures. They are Congo red negative and lack the dense amyloid cores commonly present in Alzheimer disease.
Defects in APP are the cause of amyloidosis cerebroarterial Italian type (AMYLCAIT) [MIM:605714]. AMYLCAIT is a hereditary localized amyloidosis due to amyloid-beta A4 peptide(s) deposition in the cerebral vessels, resulting in cerebral amyloid angiopathy. Amyloid is not found outside the nervous system. It is a condition very similar to AMYLCAD, but the clinical course is less severe. Patients manifest mild cognitive decline, recurrent strokes, and epilepsy in some cases. There are extensive amyloid deposits in leptomeningeal and cortical vessels and, to a lesser extent, in the neuropil of the cerebral cortex, in the absence of neurofibrillary tangles.
Defects in APP are the cause of amyloidosis cerebroarterial Iowa type (AMYLCAIW) [MIM:605714]. AMYLCAIW is a hereditary amyloidosis due to amyloid-beta A4 peptide(s) deposition. Patients have progressive aphasic dementia, leukoencephalopathy, and occipital calcifications.
Similarity:Belongs to the APP family. Contains 1 BPTI/Kunitz inhibitor domain.
Database links:
Entrez Gene: 351 Human
Entrez Gene: 11820 Mouse
Entrez Gene: 54226 Rat
Omim: 104760 Human
SwissProt: P05067 Human
SwissProt: P12023 Mouse
SwissProt: P08592 Rat
Unigene: 434980 Human
Unigene: 277585 Mouse
Unigene: 2104 Rat
Important Note:This product as supplied is intended for research use only, not for use in human, therapeutic or diagnostic applications.
111β-Amyloid 也稱β-A4 蛋白、Aβ1-42,是β-澱粉樣蛋白前體(tǐ)(APP)經β和(hé)γ分泌酶分解後的産物,有(yǒu)39-43個(gè)氨基酸殘基組成。是澱粉樣蛋白的主要成分。此蛋白在大(dà)腦(nǎo)中形成不容性的沉積物(老年斑),從而具有(yǒu)特殊的AD,Down's綜合症和(hé)老年癡呆症的形态學特征。β-澱粉樣蛋白來(lái)自β-澱粉樣蛋白原,在腦(nǎo)組織的細胞外呈絲狀蛋白樣沉積,是澱粉樣結節性神經炎病變的主要蛋白成分,在神經纖維中也有(yǒu)沉積。
在老年性癡呆Alzheimer病中,大(dà)腦(nǎo)皮質中特征性地出現β-澱粉樣蛋白沉積形成的老年斑。主要用于老年性癡呆症病人(rén)大(dà)腦(nǎo)組織噬斑中澱粉樣物質的檢測。必要時(shí)石蠟組織切片用98-100%甲酸處理(lǐ)2-3分鍾。
222
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凡以任何方式登錄本網站(zhàn)或直接、間(jiān)接使用本網站(zhàn)資料者,視(shì)為(wèi)自願接受本網站(zhàn)聲明(míng)的約束。
通(tōng)用銷售條款
一. 買方對産品的使用:産品應當用于實驗室研究目的,不可(kě)用作(zuò)其他用途(包括但(dàn)不限于:體(tǐ)外診斷、食品、藥物、醫(yī)療器(qì)械、人(rén)用或獸用治療、化妝品或其他商業用途)。購買方應明(míng)确清楚知道(dào)此聲明(míng),并嚴格遵守。如有(yǒu)任何因購買方隐瞞真實購買意圖,由此引起的法律責任以及一切法律後果,由購買方承擔。
二. 準确訂貨:下訂單時(shí),買方應預先仔細審閱産品的技(jì)術(shù)指标,确認無誤。不詳之處應立即查詢。訂單及産品一經發出,即視(shì)為(wèi)買方認可(kě)有(yǒu)關産品的技(jì)術(shù)指标。
三. 質量責任:我司保證所供産品質量與随貨COA所列标準相符。買方應以産品制(zhì)造商的标準作(zuò)為(wèi)驗收标準。鑒于化學品的特殊性,賣方對未使用之前的産品質量負責,對化學品的應用不負有(yǒu)任何直接與間(jiān)接的責任。賣方提醒買方:在做(zuò)實驗之前,預先按照技(jì)術(shù)規範檢驗産品質量。在産品開(kāi)始使用之後,買方對應用及其結果負有(yǒu)全部責任。若有(yǒu)質量異議,買方需在收到貨物後10個(gè)工作(zuò)日內(nèi)書(shū)面通(tōng)知賣方,過期無效。
四. 有(yǒu)限保證:在适用法律允許的最大(dà)限度內(nèi),賣方提供的産品均“按現狀條件”提供給買方,賣方不作(zuò)對産品和(hé)/或其使用的各種明(míng)示或默示的保證(包括但(dàn)不限于對适銷性、适合用于特殊用途及不侵權的所有(yǒu)明(míng)示或默示保證)或賣方産品會(huì)達到任何特定結果或不會(huì)被中斷或不會(huì)有(yǒu)錯誤的保證。
五. 責任限制(zhì):在适用法律允許的最大(dà)限度內(nèi),賣方不對以任何方式由本合同、賣方産品或使用賣方産品引起的或與此有(yǒu)關的任何利潤或收入損失或其他後果性損失、随附性損失、特殊損失、懲罰性損失或任何其他間(jiān)接損失或損害承擔責任。在适用法律允許的最大(dà)限度內(nèi),賣方的最高(gāo)賠償限額為(wèi)買方就所涉及的賣方産品實際支付給賣方的價格。
六. 如賣方因不可(kě)抗拒力原因無法供貨,賣方将及時(shí)通(tōng)知買方,雙方将視(shì)情況決定部分不履行(xíng)、全部不履行(xíng)或延期履行(xíng);如供貨期限屆滿日為(wèi)國內(nèi)外重大(dà)節日或國家(jiā)法定假日,則供貨期限順延;若因缺貨導緻延期交貨或無法供貨,賣方将及時(shí)告知買方,并不視(shì)為(wèi)賣方違約。不可(kě)抗力:因火(huǒ)災、洪水(shuǐ)、風暴、爆炸、恐怖事件、戰争、政府行(xíng)為(wèi)或任何其他賣方無法預見、無法避免和(hé)無法克服的事件造成延期交貨或無法交貨的,賣方不承擔任何責任。
訂購方式:
(1)直接注冊www.ruichubio.com網站(zhàn)會(huì)員後直接在線訂購支持支付寶、微信和(hé)公務卡支付;
(2)撥打021-59145618訂購熱線訂購;
(3)登錄www.ruichubio.com下載中心下載訂購單發送至:order@ruichubio.com訂購
注:在郵件确認合同或訂購單情況下,可(kě)以貨物和(hé)發票(piào)一起寄送,對公轉賬。
發票(piào):
本公司出具增值稅普通(tōng)發票(piào)和(hé)增值稅專用發票(piào),适合您報銷。發票(piào)面額為(wèi)含稅後的貨物價格和(hé)運費,請(qǐng)您放心購買,我們會(huì)将運費開(kāi)進發票(piào)裏。請(qǐng)在拍下時(shí)在備注一欄裏寫上(shàng)發票(piào)擡頭。
支付:
開(kāi)票(piào)賬戶:
公司名稱 上海晨栀生物科技有限公司
電(diàn)話(huà) 021-60543596
納稅人(rén)識别号 91310116057685530X
開(kāi)戶銀行(xíng)全稱 中國銀行(xíng)股份有(yǒu)限公司上(shàng)海市長甯支行(xíng)
帳号 454663168779
支付寶轉賬請(qǐng)支付到如下賬戶
帳 戶 名 上海晨栀生物科技有限公司
賬 号 epay@ruichubio.com
為(wèi)了方便高(gāo)校(xiào)科研單位公務卡結算(suàn),本網站(zhàn)開(kāi)通(tōng)了公務卡支付。可(kě)以在線下單選擇支付寶付款,登錄支付寶賬号添加銀行(xíng)卡(輸入公務卡号就可(kě)以)(公務卡一般就是信用卡,請(qǐng)按信用卡支付方式支付)。
運輸:
(1)生(shēng)物試劑需要冷凍運輸,運輸需要泡沫盒和(hé)一定量的冰袋(特殊商品需要幹冰),運費金額會(huì)開(kāi)進發票(piào)裏。運費以顯示為(wèi)準
(2)常規試劑采用快遞,運費以顯示為(wèi)準。
(3)大(dà)物件一般默認發德邦物流,運費需聯系客服計(jì)算(suàn)。
本網站(zhàn)所提供的信息,隻供參考之用。
本網站(zhàn)及其雇員一概毋須以任何方式就任何信息傳遞或傳送的失誤、不準确或錯誤對用戶或任何其他人(rén)士負任何直接或間(jiān)接的責任。
在法律允許的範圍內(nèi),本網站(zhàn)在此聲明(míng),不承擔用戶或任何人(rén)士就使用或未能使用本網站(zhàn)所提供的信息或任何鏈接或項目所引緻的任何直接、間(jiān)接、附帶、從屬、特殊、懲罰性或懲戒性的損害賠償(包括但(dàn)不限于收益、預期利潤的損失或失去的業務、未實現預期的節省)。
本網站(zhàn)所提供的信息,若在任何司法管轄地區(qū)供任何人(rén)士使用或分發給任何人(rén)士時(shí)會(huì)違反該司法管轄地區(qū)的法律或條例的規定或會(huì)導緻本網站(zhàn)或其第三方代理(lǐ)人(rén)受限于該司法管轄地區(qū)內(nèi)的任何監管規定時(shí),則該等信息不宜在該司法管轄地區(qū)供該等任何人(rén)士使用或分發給該等任何人(rén)士。用戶須自行(xíng)保證不會(huì)受限于任何限制(zhì)或禁止用戶使用或分發本網站(zhàn)所提供信息的當地的規定。
本網站(zhàn)圖片,文字之類版權申明(míng),因為(wèi)網站(zhàn)可(kě)以由注冊用戶自行(xíng)上(shàng)傳圖片或文字,本網站(zhàn)無法鑒别所上(shàng)傳圖片或文字的知識版權,如果侵犯,請(qǐng)及時(shí)通(tōng)知我們,本網站(zhàn)将在第一時(shí)間(jiān)及時(shí)删除。
凡以任何方式登錄本網站(zhàn)或直接、間(jiān)接使用本網站(zhàn)資料者,視(shì)為(wèi)自願接受本網站(zhàn)聲明(míng)的約束。
通(tōng)用銷售條款
一. 買方對産品的使用:産品應當用于實驗室研究目的,不可(kě)用作(zuò)其他用途(包括但(dàn)不限于:體(tǐ)外診斷、食品、藥物、醫(yī)療器(qì)械、人(rén)用或獸用治療、化妝品或其他商業用途)。購買方應明(míng)确清楚知道(dào)此聲明(míng),并嚴格遵守。如有(yǒu)任何因購買方隐瞞真實購買意圖,由此引起的法律責任以及一切法律後果,由購買方承擔。
二. 準确訂貨:下訂單時(shí),買方應預先仔細審閱産品的技(jì)術(shù)指标,确認無誤。不詳之處應立即查詢。訂單及産品一經發出,即視(shì)為(wèi)買方認可(kě)有(yǒu)關産品的技(jì)術(shù)指标。
三. 質量責任:我司保證所供産品質量與随貨COA所列标準相符。買方應以産品制(zhì)造商的标準作(zuò)為(wèi)驗收标準。鑒于化學品的特殊性,賣方對未使用之前的産品質量負責,對化學品的應用不負有(yǒu)任何直接與間(jiān)接的責任。賣方提醒買方:在做(zuò)實驗之前,預先按照技(jì)術(shù)規範檢驗産品質量。在産品開(kāi)始使用之後,買方對應用及其結果負有(yǒu)全部責任。若有(yǒu)質量異議,買方需在收到貨物後10個(gè)工作(zuò)日內(nèi)書(shū)面通(tōng)知賣方,過期無效。
四. 有(yǒu)限保證:在适用法律允許的最大(dà)限度內(nèi),賣方提供的産品均“按現狀條件”提供給買方,賣方不作(zuò)對産品和(hé)/或其使用的各種明(míng)示或默示的保證(包括但(dàn)不限于對适銷性、适合用于特殊用途及不侵權的所有(yǒu)明(míng)示或默示保證)或賣方産品會(huì)達到任何特定結果或不會(huì)被中斷或不會(huì)有(yǒu)錯誤的保證。
五. 責任限制(zhì):在适用法律允許的最大(dà)限度內(nèi),賣方不對以任何方式由本合同、賣方産品或使用賣方産品引起的或與此有(yǒu)關的任何利潤或收入損失或其他後果性損失、随附性損失、特殊損失、懲罰性損失或任何其他間(jiān)接損失或損害承擔責任。在适用法律允許的最大(dà)限度內(nèi),賣方的最高(gāo)賠償限額為(wèi)買方就所涉及的賣方産品實際支付給賣方的價格。
六. 如賣方因不可(kě)抗拒力原因無法供貨,賣方将及時(shí)通(tōng)知買方,雙方将視(shì)情況決定部分不履行(xíng)、全部不履行(xíng)或延期履行(xíng);如供貨期限屆滿日為(wèi)國內(nèi)外重大(dà)節日或國家(jiā)法定假日,則供貨期限順延;若因缺貨導緻延期交貨或無法供貨,賣方将及時(shí)告知買方,并不視(shì)為(wèi)賣方違約。不可(kě)抗力:因火(huǒ)災、洪水(shuǐ)、風暴、爆炸、恐怖事件、戰争、政府行(xíng)為(wèi)或任何其他賣方無法預見、無法避免和(hé)無法克服的事件造成延期交貨或無法交貨的,賣方不承擔任何責任。
訂購方式:
(1)直接注冊www.ruichubio.com網站(zhàn)會(huì)員後直接在線訂購支持支付寶、微信和(hé)公務卡支付;
(2)撥打021-59145618訂購熱線訂購;
(3)登錄www.ruichubio.com下載中心下載訂購單發送至:order@ruichubio.com訂購
注:在郵件确認合同或訂購單情況下,可(kě)以貨物和(hé)發票(piào)一起寄送,對公轉賬。
發票(piào):
本公司出具增值稅普通(tōng)發票(piào)和(hé)增值稅專用發票(piào),适合您報銷。發票(piào)面額為(wèi)含稅後的貨物價格和(hé)運費,請(qǐng)您放心購買,我們會(huì)将運費開(kāi)進發票(piào)裏。請(qǐng)在拍下時(shí)在備注一欄裏寫上(shàng)發票(piào)擡頭。
支付:
開(kāi)票(piào)賬戶:
公司名稱 上海晨栀生物科技有限公司
電(diàn)話(huà) 021-60543596
納稅人(rén)識别号 91310116057685530X
開(kāi)戶銀行(xíng)全稱 中國銀行(xíng)股份有(yǒu)限公司上(shàng)海市長甯支行(xíng)
帳号 454663168779
帳 戶 名 上海晨栀生物科技有限公司
賬 号 epay@ruichubio.com
為(wèi)了方便高(gāo)校(xiào)科研單位公務卡結算(suàn),本網站(zhàn)開(kāi)通(tōng)了公務卡支付。可(kě)以在線下單選擇支付寶付款,登錄支付寶賬号添加銀行(xíng)卡(輸入公務卡号就可(kě)以)(公務卡一般就是信用卡,請(qǐng)按信用卡支付方式支付)。
運輸:
(1)生(shēng)物試劑需要冷凍運輸,運輸需要泡沫盒和(hé)一定量的冰袋(特殊商品需要幹冰),運費金額會(huì)開(kāi)進發票(piào)裏。運費以顯示為(wèi)準
(2)常規試劑采用快遞,運費以顯示為(wèi)準。
(3)大(dà)物件一般默認發德邦物流,運費需聯系客服計(jì)算(suàn)。